ID A0A1H8HYK6_9BURK Unreviewed; 427 AA.
AC A0A1H8HYK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=STE24 endopeptidase {ECO:0000313|EMBL:SEN61151.1};
GN ORFNames=SAMN02745977_01643 {ECO:0000313|EMBL:SEN61151.1};
OS Brachymonas denitrificans DSM 15123.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Brachymonas.
OX NCBI_TaxID=1121117 {ECO:0000313|EMBL:SEN61151.1, ECO:0000313|Proteomes:UP000199531};
RN [1] {ECO:0000313|EMBL:SEN61151.1, ECO:0000313|Proteomes:UP000199531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15123 {ECO:0000313|EMBL:SEN61151.1,
RC ECO:0000313|Proteomes:UP000199531};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; FOCW01000003; SEN61151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8HYK6; -.
DR STRING; 1121117.SAMN02745977_01643; -.
DR Proteomes; UP000199531; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000199531};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..214
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 217..424
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 427 AA; 48323 MW; 196E0EE0FE101F19 CRC64;
MDAQLFDISY LNLFTGLFVV VLLAGMLVRF WLAGRQMRHV AWRREHVPEA FAGVISQAAH
QKAAAYTIAK NQFDLWSSVY SAAILIGWTL LGGLGLLNYT LLERIEHPMW QQLSLLAVFF
LINGLLELPL GWFQTFRLEE RFGFNKSTIG LWLGDIVKGT VMAAVIGLPL AALFLWLMQE
AGSLWWLWAW AIWVVFNLLL MVIFPTFIAP LFNKFKPLED GELAQRVQQL MQRCGFNAKG
LFVMDGSKRS AHANAYFTGL GHSKRVVFFD TLLARLQPDE VEAVLAHELG HFHFRHIAKR
LIAMFALSLA AFALLGWLYN QVWFYTGLGV VPNMMSPNAA LALILFMLVT PVFGYFLSPL
MAQLSRKHEF EADAYAVRQT GNKALPDALL KLYEDNASTL TPDPLYVKWY YSHPPASERL
ARMAQAA
//
